Evidence map›Paper›PMID 35140183›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Nonenzymatic assembly of active chimeric ribozymes from aminoacylated RNA oligonucleotides.

Aleksandar Radakovic, Saurja DasGupta, Tom H Wright, Harry R M Aitken, Jack W Szostak

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Efficient Assembly of Functional RNA byJournal of the American Chemical Society · 2025
    Article
  2. Article
  3. Stereoselectivity of Aminoacyl-RNA Loop-Closing Ligation.Journal of the American Chemical Society · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. A potential role for RNA aminoacylation prior to its role in peptide synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Template-Free Assembly of Functional RNAs by Loop-Closing Ligation.Journal of the American Chemical Society · 2022
    Article
  12. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Aleksandar RadakovicHHMI, Massachusetts General Hospital, Boston, MA 02114.ORCID 0000-0003-3794-3822
Saurja DasGuptaHHMI, Massachusetts General Hospital, Boston, MA 02114.
Tom H WrightHHMI, Massachusetts General Hospital, Boston, MA 02114.ORCID 0000-0003-2231-8223
Harry R M AitkenHHMI, Massachusetts General Hospital, Boston, MA 02114.
Jack W SzostakHHMI, Massachusetts General Hospital, Boston, MA 02114; szostak@molbio.mgh.harvard.edu.ORCID 0000-0003-4131-1203
Harvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminoacylated transfer RNAs, which harbor a covalent linkage between amino acids and RNA, are a universally conserved feature of life. Because they are essential substrates for ribosomal translation, aminoacylated oligonucleotides must have been present in the RNA world prior to the evolution of the ribosome. One possibility we are exploring is that the aminoacyl ester linkage served another function before being recruited for ribosomal protein synthesis. The nonenzymatic assembly of ribozymes from short RNA oligomers under realistic conditions remains a key challenge in demonstrating a plausible pathway from prebiotic chemistry to the RNA world. Here, we show that aminoacylated RNAs can undergo template-directed assembly into chimeric amino acid-RNA polymers that are active ribozymes. We demonstrate that such chimeric polymers can retain the enzymatic function of their all-RNA counterparts by generating chimeric hammerhead, RNA ligase, and aminoacyl transferase ribozymes. Amino acids with diverse side chains form linkages that are well tolerated within the RNA backbone and, in the case of an aminoacyl transferase, even in its catalytic center, potentially bringing novel functionalities to ribozyme catalysis. Our work suggests that aminoacylation chemistry may have played a role in primordial ribozyme assembly. Increasing the efficiency of this process provides an evolutionary rationale for the emergence of sequence and amino acid-specific aminoacyl-RNA synthetase ribozymes, which could then have generated the substrates for ribosomal protein synthesis.

Indexed as

Base SequenceDNANucleic Acid ConformationRNA, CatalyticRNA, TransferTransfer RNA AminoacylationDNARNA, CatalyticRNA, TransferaminoacylationribosomeribozymesRNAtranslation

Identifiers

PMID35140183
PMCPMC8851484
OpenAlexW4220832067

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.